ID   RNKB_CERCA              Reviewed;          95 AA.
AC   Q7Z0Q2; A6PVB5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Ribonuclease kappa-B;
DE            Short=RNase K-B;
DE            Short=RNase kappa-B;
DE            EC=3.1.-.-;
DE   AltName: Full=Cc RNase;
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, ENZYME ACTIVITY, AND
RP   ACTIVITY REGULATION.
RX   PubMed=12799437; DOI=10.1093/nar/gkg414;
RA   Rampias T.N., Sideris D.C., Fragoulis E.G.;
RT   "Cc RNase: the Ceratitis capitata ortholog of a novel highly conserved
RT   protein family in metazoans.";
RL   Nucleic Acids Res. 31:3092-3100(2003).
CC   -!- FUNCTION: Endoribonuclease which displays activity against poly(C) and
CC       poly(U) synthetic substrates, as well as rRNA.
CC       {ECO:0000269|PubMed:12799437}.
CC   -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Hg(2+), while it is
CC       unaffected by Ca(2+). {ECO:0000269|PubMed:12799437}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNase K family. {ECO:0000305}.
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DR   EMBL; AJ441124; CAD29629.1; -; mRNA.
DR   EMBL; AJ874688; CAI44684.1; -; Genomic_DNA.
DR   EMBL; AJ874689; CAI44685.1; -; mRNA.
DR   EMBL; AJ874690; CAI44686.1; -; Genomic_DNA.
DR   RefSeq; NP_001266335.1; NM_001279406.1.
DR   AlphaFoldDB; Q7Z0Q2; -.
DR   SMR; Q7Z0Q2; -.
DR   GeneID; 101448341; -.
DR   KEGG; ccat:101448341; -.
DR   OrthoDB; 1615928at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR   InterPro; IPR026770; RNase_K.
DR   PANTHER; PTHR31733; PTHR31733; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Membrane; Nuclease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..95
FT                   /note="Ribonuclease kappa-B"
FT                   /id="PRO_0000344227"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   95 AA;  10611 MW;  737D1107AE9D98C6 CRC64;
     MKICGPKLSL CGLIISVWGI IQLVLMGLFF YINSVALIED LPIDEEFNSV EEFYTAATSA
     YNQNAYNCWI AACIYVLTLL LSAQQFYVNS RATAN